Cloning and sequence analysis of a polyurethane esterase of Comamonas acidovorans TB-35

Nomura, Nobuhiko; Shigeno-Akutsu, Yukie; Nakajima-Kambe, Toshiaki; Nakahara, Tadaatsu

doi:10.1016/s0922-338x(99)89001-1

Cited by 66 publications

(38 citation statements)

References 35 publications

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“…The authors created kanamycin insertion mutations of PueA and PueB to study growth of the P. chlororaphis mutants on polyurethane. The optimum pH for this enzyme was 6.5, and the optimum temperature was 45 C. The structural gene (Pud A) which encodes PUR esterase has also been cloned in Escherichia coli and its primary structure has also been analyzed by Nomura et al 80 The Results from this have demonstrated that each residue in the Ser-His-Glu catalytic triad is in fact essential for enzymatic activity. Thus, growth studies were performed to compare the effects of the PueA-decient strain and the PueB decient strain with the wild type strain in polyurethane utilization.…”

Section: Biodegradation Of Polyurethane By Bacteriamentioning

confidence: 99%

New insights into the microbial degradation of polyurethanes

Mahajan¹,

Gupta²

2015

RSC Adv.

111

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Section: Biodegradation Of Polyurethane By Bacteriamentioning

confidence: 99%

New insights into the microbial degradation of polyurethanes

Mahajan¹,

Gupta²

2015

RSC Adv.

111

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“…A cell membrane-bound enzyme (PUR esterase, 548 amino acids, 62 kDa) was extracted from bacterium Comamonas acidovorans TB-35 (65). The gene encoding this enzyme has been identified as pudA, which consists of 1644-bp nucleotides with a putative ATG initiation codon (66). Similarly, an extracellular enzyme (PUR esterase, 617 amino acids, 65 kDa) was extracted from bacterium Pseudomonas chlororaphis (67).…”

Section: Polyurethanementioning

confidence: 99%

A review of biodegradation of synthetic plastic and foams

Gautam¹,

Bassi²,

Yanful³

2007

Appl Biochem Biotechnol

170

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Synthetic polymeric foams have pervaded every aspect of modern life. Although foams provide numerous benefits, they also cause a significant environmental litter problem because of their recalcitrant and xenobiotic nature. Biodegradation may provide solution to the problem, but not enough is known about the biodegradation process of synthetic plastic and plasticbased foams. This review has been written to provide an overview of the current state of plastic foam biodegradation. Several biodegradation pathways of a few select synthetic polymers are also presented along with a discussion on some of the physico-chemical factors that can influence the biodegradation of plastic foams.

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“…Several Pseudomonas species including Pseudomonas chlororaphis, Pseudomonas aeruginosa, and Pseudomonas fluorescens have been shown to degrade a model polyester PU, Impranil DLN (Impranil) (4)(5)(6). Three PU-degrading enzymes have been purified and characterized from some of these strains, including polyurethane esterases A (PueA) and B (PueB) from Pseudomonas chlororaphis (5,9) and polyurethane lipase (PulA) from P. fluorescens (5,(9)(10)(11). Although they are often referred to as "polyurethanases," these enzymes are more accurately classified as extracellular lipases and esterases.…”

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confidence: 99%

Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5

Hung

Zingarelli

Nadeau

et al. 2016

Appl Environ Microbiol

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Polyester polyurethane (PU) coatings are widely used to help protect underlying structural surfaces but are susceptible to biological degradation. PUs are susceptible to degradation by Pseudomonas species, due in part to the degradative activity of secreted hydrolytic enzymes. Microorganisms often respond to environmental cues by secreting enzymes or secondary metabolites to benefit their survival. This study investigated the impact of exposing several Pseudomonas strains to select carbon sources on the degradation of the colloidal polyester polyurethane Impranil DLN (Impranil). The prototypic Pseudomonas protegens strain Pf-5 exhibited Impranil-degrading activities when grown in sodium citrate but not in glucose-containing medium. Glucose also inhibited the induction of Impranil-degrading activity by citrate-fed Pf-5 in a dose-dependent manner. Biochemical and mutational analyses identified two extracellular lipases present in the Pf-5 culture supernatant (PueA and PueB) that were involved in degradation of Impranil. Deletion of the pueA gene reduced Impranil-clearing activities, while pueB deletion exhibited little effect. Removal of both genes was necessary to stop degradation of the polyurethane. Bioinformatic analysis showed that putative Cbr/Hfq/Crc-mediated regulatory elements were present in the intergenic sequences upstream of both pueA and pueB genes. Our results confirmed that both PueA and PueB extracellular enzymes act in concert to degrade Impranil. Furthermore, our data showed that carbon sources in the growth medium directly affected the levels of Impranil-degrading activity but that carbon source effects varied among Pseudomonas strains. This study uncovered an intricate and complicated regulation of P. protegens PU degradation activity controlled by carbon catabolite repression. IMPORTANCEPolyurethane (PU) coatings are commonly used to protect metals from corrosion. Microbiologically induced PU degradation might pose a substantial problem for the integrity of these coatings. Microorganisms from diverse genera, including pseudomonads, possess the ability to degrade PUs via various means. This work identified two extracellular lipases, PueA and PueB, secreted by P. protegens strain Pf-5, to be responsible for the degradation of a colloidal polyester PU, Impranil. This study also revealed that the expression of the degradative activity by strain Pf-5 is controlled by glucose carbon catabolite repression. Furthermore, this study showed that the Impranil-degrading activity of many other Pseudomonas strains could be influenced by different carbon sources. This work shed light on the carbon source regulation of PU degradation activity among pseudomonads and identified the polyurethane lipases in P. protegens.

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Cloning and sequence analysis of a polyurethane esterase of Comamonas acidovorans TB-35

Cited by 66 publications

References 35 publications

New insights into the microbial degradation of polyurethanes

New insights into the microbial degradation of polyurethanes

A review of biodegradation of synthetic plastic and foams

Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5

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